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| [[Image:1phr.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1phr| PDB=1phr | SCENE= }} | | {{STRUCTURE_1phr| PDB=1phr | SCENE= }} |
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| '''THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE'''
| | ===THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE=== |
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| ==Overview==
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| Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8052313}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8052313 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8052313}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Taddei, N.]] | | [[Category: Taddei, N.]] |
| [[Category: Phosphotyrosine protein phosphatase]] | | [[Category: Phosphotyrosine protein phosphatase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:06:01 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:54:42 2008'' |
